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Protein

Chemotaxis response regulator protein-glutamate methylesterase

Gene

cheB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the modulation of the chemotaxis system; catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR.

Catalytic activityi

Protein L-glutamate O5-methyl ester + H2O = protein L-glutamate + methanol.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei164By similarity1
Active sitei190By similarity1
Active sitei286By similarity1

GO - Molecular functioni

  • deaminase binding Source: CAFA
  • phosphorelay response regulator activity Source: InterPro
  • protein-glutamate methylesterase activity Source: CAFA

GO - Biological processi

  • chemotaxis Source: EcoliWiki
  • protein deamination Source: CAFA
  • protein demethylation Source: CAFA

Keywordsi

Molecular functionHydrolase
Biological processChemotaxis

Enzyme and pathway databases

BioCyciEcoCyc:CHEB-MONOMER
MetaCyc:CHEB-MONOMER
BRENDAi3.1.1.61 2026

Names & Taxonomyi

Protein namesi
Recommended name:
Chemotaxis response regulator protein-glutamate methylesterase (EC:3.1.1.61)
Gene namesi
Name:cheB
Ordered Locus Names:b1883, JW1872
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10147 cheB

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • plasma membrane Source: CAFA

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001579921 – 349Chemotaxis response regulator protein-glutamate methylesteraseAdd BLAST349

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei564-aspartylphosphateBy similarity1

Post-translational modificationi

Phosphorylated by CheA. Phosphorylation suppresses the inhibitory activity of the N-terminal domain.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP07330
PRIDEiP07330

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
cheAP073633EBI-1125895,EBI-1026773

GO - Molecular functioni

  • deaminase binding Source: CAFA

Protein-protein interaction databases

BioGridi4260716, 222 interactors
DIPiDIP-9272N
IntActiP07330, 10 interactors
STRINGi316385.ECDH10B_2024

Structurei

3D structure databases

ProteinModelPortaliP07330
SMRiP07330
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 122Response regulatoryPROSITE-ProRule annotationAdd BLAST118
Domaini152 – 344CheB-type methylesteraseAdd BLAST193

Domaini

The N-terminal regulatory domain inhibits the activity of the C-terminal effector domain.

Phylogenomic databases

eggNOGiENOG4105CMP Bacteria
COG2201 LUCA
HOGENOMiHOG000151423
InParanoidiP07330
KOiK03412
OMAiMLEMHRA
PhylomeDBiP07330

Family and domain databases

CDDicd16432 CheB_Rec, 1 hit
cd00156 REC, 1 hit
Gene3Di3.40.50.180, 1 hit
HAMAPiMF_00099 CheB_methylest, 1 hit
InterProiView protein in InterPro
IPR035909 CheB_C
IPR011006 CheY-like_superfamily
IPR008248 Sig_transdc_resp-reg_CheB
IPR000673 Sig_transdc_resp-reg_Me-estase
IPR001789 Sig_transdc_resp-reg_receiver
PfamiView protein in Pfam
PF01339 CheB_methylest, 1 hit
PF00072 Response_reg, 1 hit
PIRSFiPIRSF000876 RR_chemtxs_CheB, 1 hit
SMARTiView protein in SMART
SM00448 REC, 1 hit
SUPFAMiSSF52172 SSF52172, 1 hit
SSF52738 SSF52738, 1 hit
PROSITEiView protein in PROSITE
PS50122 CHEB, 1 hit
PS50110 RESPONSE_REGULATORY, 1 hit

Sequencei

Sequence statusi: Complete.

P07330-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKIRVLSVD DSALMRQIMT EIINSHSDME MVATAPDPLV ARDLIKKFNP
60 70 80 90 100
DVLTLDVEMP RMDGLDFLEK LMRLRPMPVV MVSSLTGKGS EVTLRALELG
110 120 130 140 150
AIDFVTKPQL GIREGMLAYN EMIAEKVRTA AKASLAAHKP LSAPTTLKAG
160 170 180 190 200
PLLSSEKLIA IGASTGGTEA IRHVLQPLPL SSPALLITQH MPPGFTRSFA
210 220 230 240 250
DRLNKLCQIG VKEAEDGERV LPGHAYIAPG DRHMELSRSG ANYQIKIHDG
260 270 280 290 300
PAVNRHRPSV DVLFHSVAKQ AGRNAVGVIL TGMGNDGAAG MLAMRQAGAW
310 320 330 340
TLAQNEASCV VFGMPREAIN MGGVCEVVDL SQVSQQMLAK ISAGQAIRI
Length:349
Mass (Da):37,468
Last modified:November 1, 1997 - v3
Checksum:i6F3D1AFB8D23D3F5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96A → P in AAA23569 (PubMed:3510184).Curated1
Sequence conflicti125E → Q in AAA23569 (PubMed:3510184).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13463 Genomic DNA Translation: AAA23569.1
U00096 Genomic DNA Translation: AAC74953.1
AP009048 Genomic DNA Translation: BAA15699.1
PIRiD25195 XYECEB
RefSeqiNP_416397.1, NC_000913.3
WP_000036361.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC74953; AAC74953; b1883
BAA15699; BAA15699; BAA15699
GeneIDi946394
KEGGiecj:JW1872
eco:b1883
PATRICifig|1411691.4.peg.364

Similar proteinsi

Entry informationi

Entry nameiCHEB_ECOLI
AccessioniPrimary (citable) accession number: P07330
Secondary accession number(s): P78070
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 154 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

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